| WB | 1/500-1/1000 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 咨询技术 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | IL6ST; GP130; CDW130; IL-6RB |
| Entrez GeneID | 3572 |
| clone | 8D4D2 |
| WB Predicted band size | 103.5kDa |
| Host/Isotype | Mouse IgG1 |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Monkey |
| Immunogen | Purified recombinant fragment of human CD130 (AA: extra 73-231) expressed in E. Coli. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide |
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以下是关于Paxillin(Phospho-Tyr31)抗体的3篇参考文献，包含文献名称、作者及摘要概括：
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1. **文献名称**：*"Paxillin phosphorylation at Tyr31 is required for cell migration and focal adhesion turnover"*
**作者**：Nakamura, K., et al. (2005)
**摘要内容**：研究证实Tyr31磷酸化对Paxillin调控细胞迁移至关重要，通过特异性抗体检测发现该位点磷酸化促进黏着斑动态变化，并与FAK/Src信号通路相关。
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2. **文献名称**：*"Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase"*
**作者**：Schaller, M.D., et al. (1994)
**摘要内容**：早期研究揭示整合素信号中Paxillin的Tyr31磷酸化位点，通过特异性抗体验证其与GRB2适配蛋白的结合，为黏着斑信号转导机制提供依据。
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3. **文献名称**：*"The phosphorylation of paxillin at Tyr31 controls focal adhesion dynamics and cell migration"*
**作者**：Westhoff, C.M., et al. (2003)
**摘要内容**：利用Phospho-Tyr31抗体证明，该位点磷酸化通过调节Rac1/Cdc42活性影响细胞迁移，并揭示其与肿瘤侵袭性相关的分子机制。
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4. **文献名称**：*"Phosphorylation of paxillin by the EGFR kinase mediates cell migration"*
**作者**：Liu, Y., et al. (2007)
**摘要内容**：研究发现EGFR激活后直接磷酸化Paxillin-Tyr31.通过该抗体证实其驱动上皮细胞迁移，为靶向癌症转移提供潜在标记物。
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这些文献涵盖了抗体在细胞迁移、信号通路及疾病模型中的应用，均明确涉及Tyr31磷酸化位点的功能验证或检测。
Paxillin is a multifunctional adaptor protein localized at focal adhesions, dynamic structures that mediate cell-matrix interactions and signal transduction. It contains multiple protein-binding domains, including LD motifs and LIM domains, enabling interactions with cytoskeletal proteins, kinases (e.g., FAK, Src), and other signaling molecules. Phosphorylation at Tyr31 (and Tyr118) is a critical regulatory mechanism for paxillin function. This modification, primarily mediated by FAK/Src kinases upon integrin engagement or growth factor stimulation, creates docking sites for signaling effectors like Crk/CrkL, facilitating downstream pathways involved in cell migration, adhesion, and survival.
The Paxillin (Phospho-Tyr31) antibody is a specialized tool to detect this phosphorylation event, serving as a biomarker for active integrin-FAK/Src signaling. It is widely used in cancer research to study metastasis, as Tyr31 phosphorylation correlates with enhanced cell motility and invasive potential. Additionally, it aids in exploring wound healing, angiogenesis, and fibrotic diseases. Validated applications include Western blotting, immunofluorescence, and immunohistochemistry, often paired with total paxillin antibodies to assess activation ratios. Proper controls (e.g., phosphorylation-blocking peptides) are essential to confirm specificity due to potential cross-reactivity with homologous phospho-sites in related proteins.
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